ID CDIPT_HUMAN Reviewed; 213 AA. AC O14735; B4DUV0; H3BTV1; Q6FGU1; Q6ZN70; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000305}; DE EC=2.7.8.11 {ECO:0000269|PubMed:8110188, ECO:0000269|PubMed:9407135}; DE AltName: Full=Phosphatidylinositol synthase; DE Short=PI synthase; DE Short=PtdIns synthase; GN Name=CDIPT {ECO:0000312|HGNC:HGNC:1769}; Synonyms=PIS, PIS1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND FUNCTION. RC TISSUE=Testis; RX PubMed=9407135; DOI=10.1074/jbc.272.52.33402; RA Lykidis A., Jackson P.D., Rock C.O., Jackowski S.; RT "The role of CDP-diacylglycerol synthetase and phosphatidylinositol RT synthase activity levels in the regulation of cellular phosphatidylinositol RT content."; RL J. Biol. Chem. 272:33402-33409(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=8110188; DOI=10.1042/bj2970517; RA Antonsson B.E.; RT "Purification and characterization of phosphatidylinositol synthase from RT human placenta."; RL Biochem. J. 297:517-522(1994). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) CC as well as PtdIns:inositol exchange reaction. May thus act to reduce an CC excessive cellular PtdIns content. The exchange activity is due to the CC reverse reaction of PtdIns synthase and is dependent on CMP, which is CC tightly bound to the enzyme. {ECO:0000269|PubMed:8110188, CC ECO:0000269|PubMed:9407135}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn- CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; CC Evidence={ECO:0000269|PubMed:8110188, ECO:0000269|PubMed:9407135}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11581; CC Evidence={ECO:0000305|PubMed:9407135}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11582; CC Evidence={ECO:0000305|PubMed:9407135}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:8110188}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:8110188}; CC Note=Catalytic activity is higher with Mg(2+). CC {ECO:0000269|PubMed:8110188}; CC -!- ACTIVITY REGULATION: Inhibited by PtdIns (product inhibition), CC phosphatidylinositol phosphate, and nucleoside di- and tri-phosphates. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 9.0. {ECO:0000269|PubMed:8110188}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:8110188}; CC -!- INTERACTION: CC O14735; P41181: AQP2; NbExp=3; IntAct=EBI-358858, EBI-12701138; CC O14735; Q13520: AQP6; NbExp=3; IntAct=EBI-358858, EBI-13059134; CC O14735; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-358858, EBI-11343438; CC O14735; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-358858, EBI-12935759; CC O14735; Q8WZ55: BSND; NbExp=3; IntAct=EBI-358858, EBI-7996695; CC O14735; P11912: CD79A; NbExp=3; IntAct=EBI-358858, EBI-7797864; CC O14735; Q99675: CGRRF1; NbExp=3; IntAct=EBI-358858, EBI-2130213; CC O14735; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-358858, EBI-1045797; CC O14735; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-358858, EBI-18013275; CC O14735; P49447: CYB561; NbExp=3; IntAct=EBI-358858, EBI-8646596; CC O14735; P00387: CYB5R3; NbExp=3; IntAct=EBI-358858, EBI-1046040; CC O14735; Q6PI48: DARS2; NbExp=3; IntAct=EBI-358858, EBI-3917045; CC O14735; Q15125: EBP; NbExp=3; IntAct=EBI-358858, EBI-3915253; CC O14735; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-358858, EBI-781551; CC O14735; P34910-2: EVI2B; NbExp=3; IntAct=EBI-358858, EBI-17640610; CC O14735; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-358858, EBI-18304435; CC O14735; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-358858, EBI-17187481; CC O14735; O15552: FFAR2; NbExp=3; IntAct=EBI-358858, EBI-2833872; CC O14735; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-358858, EBI-3918971; CC O14735; P08034: GJB1; NbExp=3; IntAct=EBI-358858, EBI-17565645; CC O14735; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-358858, EBI-712073; CC O14735; Q96P66: GPR101; NbExp=3; IntAct=EBI-358858, EBI-17935713; CC O14735; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-358858, EBI-11955647; CC O14735; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-358858, EBI-13345167; CC O14735; Q8TED1: GPX8; NbExp=3; IntAct=EBI-358858, EBI-11721746; CC O14735; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-358858, EBI-18053395; CC O14735; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-358858, EBI-725665; CC O14735; P24592: IGFBP6; NbExp=3; IntAct=EBI-358858, EBI-947015; CC O14735; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-358858, EBI-10266796; CC O14735; O00180: KCNK1; NbExp=3; IntAct=EBI-358858, EBI-3914675; CC O14735; P43628: KIR2DL3; NbExp=3; IntAct=EBI-358858, EBI-8632435; CC O14735; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-358858, EBI-739832; CC O14735; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-358858, EBI-11956541; CC O14735; O14880: MGST3; NbExp=3; IntAct=EBI-358858, EBI-724754; CC O14735; Q96JA4: MS4A14; NbExp=3; IntAct=EBI-358858, EBI-12839612; CC O14735; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-358858, EBI-3923617; CC O14735; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-358858, EBI-12382569; CC O14735; P60201-2: PLP1; NbExp=3; IntAct=EBI-358858, EBI-12188331; CC O14735; Q8NC24: RELL2; NbExp=3; IntAct=EBI-358858, EBI-10269209; CC O14735; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-358858, EBI-10192441; CC O14735; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-358858, EBI-2466594; CC O14735; O95197: RTN3; NbExp=3; IntAct=EBI-358858, EBI-740467; CC O14735; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-358858, EBI-4395514; CC O14735; O00560: SDCBP; NbExp=3; IntAct=EBI-358858, EBI-727004; CC O14735; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-358858, EBI-17640454; CC O14735; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-358858, EBI-18159983; CC O14735; O60669: SLC16A7; NbExp=3; IntAct=EBI-358858, EBI-3921243; CC O14735; P30825: SLC7A1; NbExp=3; IntAct=EBI-358858, EBI-4289564; CC O14735; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-358858, EBI-12947623; CC O14735; Q9Y320: TMX2; NbExp=3; IntAct=EBI-358858, EBI-6447886; CC O14735; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-358858, EBI-13356252; CC O14735; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-358858, EBI-1055364; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:8110188}; Multi-pass membrane protein CC {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:8110188}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O14735-1; Sequence=Displayed; CC Name=2; CC IsoId=O14735-2; Sequence=VSP_013618, VSP_013619, VSP_013620; CC Name=3; CC IsoId=O14735-3; Sequence=VSP_054767; CC -!- TISSUE SPECIFICITY: Detected in placenta (at protein level). Widely CC expressed. Higher expression in adult liver and skeletal muscle, CC slightly lower levels seen in pancreas, kidney, lung, placenta, brain, CC heart, leukocyte, colon, small intestine, ovary, testis, prostate, CC thymus and spleen. In fetus, expressed in kidney, liver, lung and CC brain. {ECO:0000269|PubMed:8110188}. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF014807; AAB94860.1; -; mRNA. DR EMBL; BT007301; AAP35965.1; -; mRNA. DR EMBL; AK131349; BAD18505.1; -; mRNA. DR EMBL; AK300805; BAG62462.1; -; mRNA. DR EMBL; CR542016; CAG46813.1; -; mRNA. DR EMBL; AC120114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001444; AAH01444.1; -; mRNA. DR CCDS; CCDS10657.1; -. [O14735-1] DR CCDS; CCDS67002.1; -. [O14735-3] DR RefSeq; NP_001273514.1; NM_001286585.1. [O14735-3] DR RefSeq; NP_006310.1; NM_006319.4. [O14735-1] DR AlphaFoldDB; O14735; -. DR SMR; O14735; -. DR BioGRID; 115692; 181. DR DIP; DIP-54492N; -. DR IntAct; O14735; 116. DR MINT; O14735; -. DR STRING; 9606.ENSP00000219789; -. DR DrugBank; DB03106; scyllo-inositol. DR SwissLipids; SLP:000000533; -. DR iPTMnet; O14735; -. DR PhosphoSitePlus; O14735; -. DR SwissPalm; O14735; -. DR BioMuta; CDIPT; -. DR EPD; O14735; -. DR jPOST; O14735; -. DR MassIVE; O14735; -. DR MaxQB; O14735; -. DR PaxDb; 9606-ENSP00000219789; -. DR PeptideAtlas; O14735; -. DR ProteomicsDB; 42746; -. DR ProteomicsDB; 48197; -. [O14735-1] DR ProteomicsDB; 48198; -. [O14735-2] DR Pumba; O14735; -. DR Antibodypedia; 26862; 74 antibodies from 18 providers. DR DNASU; 10423; -. DR Ensembl; ENST00000219789.11; ENSP00000219789.6; ENSG00000103502.14. [O14735-1] DR Ensembl; ENST00000566113.5; ENSP00000457340.1; ENSG00000103502.14. [O14735-3] DR Ensembl; ENST00000569956.5; ENSP00000457339.1; ENSG00000103502.14. [O14735-1] DR Ensembl; ENST00000570016.5; ENSP00000454453.1; ENSG00000103502.14. [O14735-1] DR GeneID; 10423; -. DR KEGG; hsa:10423; -. DR MANE-Select; ENST00000219789.11; ENSP00000219789.6; NM_006319.5; NP_006310.1. DR UCSC; uc002dum.5; human. [O14735-1] DR AGR; HGNC:1769; -. DR CTD; 10423; -. DR DisGeNET; 10423; -. DR GeneCards; CDIPT; -. DR HGNC; HGNC:1769; CDIPT. DR HPA; ENSG00000103502; Low tissue specificity. DR MIM; 605893; gene. DR neXtProt; NX_O14735; -. DR OpenTargets; ENSG00000103502; -. DR PharmGKB; PA26306; -. DR VEuPathDB; HostDB:ENSG00000103502; -. DR eggNOG; KOG3240; Eukaryota. DR GeneTree; ENSGT00940000154169; -. DR HOGENOM; CLU_067602_2_0_1; -. DR InParanoid; O14735; -. DR OMA; FWFQLSM; -. DR OrthoDB; 5472855at2759; -. DR PhylomeDB; O14735; -. DR TreeFam; TF314603; -. DR BioCyc; MetaCyc:HS02513-MONOMER; -. DR BRENDA; 2.7.8.11; 2681. DR PathwayCommons; O14735; -. DR Reactome; R-HSA-1483226; Synthesis of PI. DR SignaLink; O14735; -. DR BioGRID-ORCS; 10423; 597 hits in 1173 CRISPR screens. DR ChiTaRS; CDIPT; human. DR GeneWiki; CDIPT; -. DR GenomeRNAi; 10423; -. DR Pharos; O14735; Tbio. DR PRO; PR:O14735; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O14735; Protein. DR Bgee; ENSG00000103502; Expressed in parotid gland and 207 other cell types or tissues. DR ExpressionAtlas; O14735; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB. DR Gene3D; 1.20.120.1760; -; 1. DR InterPro; IPR000462; CDP-OH_P_trans. DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom. DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS. DR InterPro; IPR014387; CDP_diag_ino_3_P_euk. DR PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1. DR PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. DR Genevisible; O14735; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Endoplasmic reticulum; KW Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; Membrane; KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..213 FT /note="CDP-diacylglycerol--inositol 3- FT phosphatidyltransferase" FT /id="PRO_0000056802" FT TOPO_DOM 1..5 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 27 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 49..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 95 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 117..139 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 161..174 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 175..195 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 196..213 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 51 FT /ligand="a CDP-1,2-diacyl-sn-glycerol" FT /ligand_id="ChEBI:CHEBI:58332" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 55 FT /ligand="a CDP-1,2-diacyl-sn-glycerol" FT /ligand_id="ChEBI:CHEBI:58332" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 61 FT /ligand="a CDP-1,2-diacyl-sn-glycerol" FT /ligand_id="ChEBI:CHEBI:58332" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT BINDING 72 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P9WPG7" FT VAR_SEQ 1..14 FT /note="MPDENIFLFVPNLI -> MLPTAAGFSIWGQVGAAREAPRCQTKISSCSCPT FT SSVSAAHGPGPNERARGLGGLPDPALSPRVPFQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013618" FT VAR_SEQ 15..59 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054767" FT VAR_SEQ 111..129 FT /note="SSVVRGSESHKMIDLSGNP -> RSAAILGAWATWRHYSGVG (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013619" FT VAR_SEQ 130..213 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013620" FT VARIANT 199 FT /note="R -> C (in dbSNP:rs1802002)" FT /id="VAR_048734" FT CONFLICT 75 FT /note="S -> P (in Ref. 3; BAG62462)" FT /evidence="ECO:0000305" SQ SEQUENCE 213 AA; 23539 MW; 7885B72EF2A88093 CRC64; MPDENIFLFV PNLIGYARIV FAIISFYFMP CCPLTASSFY LLSGLLDAFD GHAARALNQG TRFGAMLDML TDRCSTMCLL VNLALLYPGA TLFFQISMSL DVASHWLHLH SSVVRGSESH KMIDLSGNPV LRIYYTSRPA LFTLCAGNEL FYCLLYLFHF SEGPLVGSVG LFRMGLWVTA PIALLKSLIS VIHLITAARN MAALDAADRA KKK //